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Conserved domains on  [gi|1063559289|ref|WP_069419027|]
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diacylglycerol kinase family protein [Mycobacterium intermedium]

Protein Classification

diacylglycerol/lipid kinase family protein( domain architecture ID 11446635)

diacylglycerol/lipid kinase family protein may catalyze the ATP-dependent phosphorylation of diacylglycerol and/or other lipids, and is involved in the phospholipid biosynthetic process

CATH:  3.40.50.10330
EC:  2.7.1.-
Gene Ontology:  GO:0008654|GO:0001727|GO:0005524|GO:0016310
SCOP:  3001940

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
 1-321 1.20e-57

Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, General function prediction only];


:

Pssm-ID: 441205 [Multi-domain]  Cd Length: 295  Bit Score: 187.75  E-value: 1.20e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063559289   1 MRAMLIVNPIATSITPA-ARELVAHALESR-VELTVEQTAYSGHAFELGKVAAADGYDLVVVHGGDGTVSAVVNGMLGRP 78
Cdd:COG1597     3 MRALLIVNPASGRGRAArLLERLVAALRAAgLEVEVLETESPGDATELAREAAAEGADLVVAAGGDGTVNEVANGLAGTG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063559289  79 dqaapdqlranvPAVGIIPGGSANVLARALGIPTDPAAASNQLIqlldvherTGNWRRIGLIDCGEVWAIVNAGVGVDAE 158
Cdd:COG1597    83 ------------PPLGILPLGTGNDFARALGIPLDPEAALEALL--------TGRTRRIDLGRVNGRYFLNVAGIGFDAE 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063559289 159 VVAAVEEKRRQgvKVTPLNYWRIAtpVSVRFSRREPNLILELPEREPIPGVHFAWVCNTNvwTYSSNrpMVTNPGCSFET 238
Cdd:COG1597   143 VVERANRALKR--RLGKLAYVLAA--LRALLRYRPFRLRIELDGEEIEGEALLVAVGNGP--YYGGG--LRLAPDASLDD 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063559289 239 G-LGLFALTSMKLIPTIRLLRQLMAKRpkleakqLIRDDDVSYVRVTRMR----EPAAVQFDGEYLGLRETMTFREVRDI 313
Cdd:COG1597   215 GlLDVVVVRPLSRLRLLRLLPRLLRGR-------HLRHPGVRYFRAREVEiesdRPLPVQLDGEPLGLATPLEFEVLPGA 287


                  ....*...
gi 1063559289 314 LPVVAPPS 321
Cdd:COG1597   288 LRVLVPAD 295
 
Name Accession Description Interval E-value
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
 1-321 1.20e-57

Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, General function prediction only];


Pssm-ID: 441205 [Multi-domain]  Cd Length: 295  Bit Score: 187.75  E-value: 1.20e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063559289   1 MRAMLIVNPIATSITPA-ARELVAHALESR-VELTVEQTAYSGHAFELGKVAAADGYDLVVVHGGDGTVSAVVNGMLGRP 78
Cdd:COG1597     3 MRALLIVNPASGRGRAArLLERLVAALRAAgLEVEVLETESPGDATELAREAAAEGADLVVAAGGDGTVNEVANGLAGTG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063559289  79 dqaapdqlranvPAVGIIPGGSANVLARALGIPTDPAAASNQLIqlldvherTGNWRRIGLIDCGEVWAIVNAGVGVDAE 158
Cdd:COG1597    83 ------------PPLGILPLGTGNDFARALGIPLDPEAALEALL--------TGRTRRIDLGRVNGRYFLNVAGIGFDAE 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063559289 159 VVAAVEEKRRQgvKVTPLNYWRIAtpVSVRFSRREPNLILELPEREPIPGVHFAWVCNTNvwTYSSNrpMVTNPGCSFET 238
Cdd:COG1597   143 VVERANRALKR--RLGKLAYVLAA--LRALLRYRPFRLRIELDGEEIEGEALLVAVGNGP--YYGGG--LRLAPDASLDD 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063559289 239 G-LGLFALTSMKLIPTIRLLRQLMAKRpkleakqLIRDDDVSYVRVTRMR----EPAAVQFDGEYLGLRETMTFREVRDI 313
Cdd:COG1597   215 GlLDVVVVRPLSRLRLLRLLPRLLRGR-------HLRHPGVRYFRAREVEiesdRPLPVQLDGEPLGLATPLEFEVLPGA 287


                  ....*...
gi 1063559289 314 LPVVAPPS 321
Cdd:COG1597   288 LRVLVPAD 295
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
 2-145 2.24e-31

Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts as a protein kinase C activator. The catalytic domain is assumed from the finding of bacterial homologs. YegS is the Escherichia coli protein in this family whose crystal structure reveals an active site in the inter-domain cleft formed by four conserved sequence motifs, revealing a novel metal-binding site. The residues of this site are conserved across the family.


Pssm-ID: 425868 [Multi-domain]  Cd Length: 125  Bit Score: 114.22  E-value: 2.24e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063559289   2 RAMLIVNPiaTSITPAARELVAHA---LESR-VELTVEQTAYSGHAFELGKVAAADGYDLVVVHGGDGTVSAVVNGMLGR 77
Cdd:pfam00781   1 KLLVIVNP--KSGGGKGKKLLRKVrplLNKAgVEVELVLTEGPGDALELAREAAEDGYDRIVVAGGDGTVNEVLNGLAGL 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063559289  78 PDQaapdqlranvPAVGIIPGGSANVLARALGIPTDPAAASNQLIQlldvhertGNWRRiglIDCGEV 145
Cdd:pfam00781  79 ATR----------PPLGIIPLGTGNDFARALGIPGDPEEALEAILK--------GQTRP---VDVGKV 125
PRK00861 PRK00861
putative lipid kinase; Reviewed
 2-171 4.54e-20

putative lipid kinase; Reviewed


Pssm-ID: 234850 [Multi-domain]  Cd Length: 300  Bit Score: 88.53  E-value: 4.54e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063559289   2 RAMLIVNPIATSITPAAR-ELVAHALESRVELTVEQTAYSGHAFELGKVAAADGYDLVVVHGGDGTVSAVVNGMLGrpdq 80
Cdd:PRK00861    4 SACLIFNPVAGQGNPEVDlALIRAILEPEMDLDIYLTTPEIGADQLAQEAIERGAELIIASGGDGTLSAVAGALIG---- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063559289  81 aapdqlrANVPaVGIIPGGSANVLARALGIPTDPAAASNQLIQlldvhertGNWRRIGLIDCGEVWAIVNAGVGVDAEVV 160
Cdd:PRK00861   80 -------TDIP-LGIIPRGTANAFAAALGIPDTIEEACRTILQ--------GKTRRVDVAYCNGQPMILLAGIGFEAETV 143

                         170
                  ....*....|...
gi 1063559289 161 --AAVEEKRRQGV 171
Cdd:PRK00861  144 eeADREAKNRFGI 156
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 5-127 1.29e-17

Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger that acts as a protein kinase C activator. DAG can be produced from the hydrolysis of phosphatidylinositol 4,5-bisphosphate (PIP2) by a phosphoinositide-specific phospholipase C and by the degradation of phosphatidylcholine (PC) by a phospholipase C or the concerted actions of phospholipase D and phosphatidate phosphohydrolase. This domain is presumed to be the catalytic domain. Bacterial homologues areknown.


Pssm-ID: 214487 [Multi-domain]  Cd Length: 124  Bit Score: 77.72  E-value: 1.29e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063559289    5 LIVNPIAT-----SITPAARELVAHALesrveltVEQTAYSGHAFELGKVAAADGYDLVVVHGGDGTVSAVVNGMLGRPD 79
Cdd:smart00046   2 VFVNPKSGggkgeKLLRKFRLLLNPRQ-------VFDLTKKGPAVALVIFRDVPDFNRVLVCGGDGTVGWVLNALDKREL 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1063559289   80 QAAPdqlranvPAVGIIPGGSANVLARALGIPTDPAAAsNQLIQLLDV 127
Cdd:smart00046  75 PLPE-------PPVAVLPLGTGNDLARSLGWGGGYDGE-KLLKTLRDA 114
TIGR00147 TIGR00147
lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been ...
 2-300 2.97e-15

lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been purified and shown to have phosphatidylglycerol kinase activity. The member from M. tuberculosis, Rv2252, has diacylglycerol kinase activity. BmrU from B. subtilis is in an operon with multidrug efflux transporter Bmr, but is uncharacterized. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 161732 [Multi-domain]  Cd Length: 293  Bit Score: 74.85  E-value: 2.97e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063559289   2 RAMLIVNPIA--TSITPAARELVAHALESRVELTVEQTAYSGHAFELGKVAAADGYDLVVVHGGDGTVSAVVNGMlgrpd 79
Cdd:TIGR00147   3 EAPAILNPTAgkSNDNKPLREVIMLLREEGMEIHVRVTWEKGDAARYVEEARKFGVDTVIAGGGDGTINEVVNAL----- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063559289  80 qAAPDqlraNVPAVGIIPGGSANVLARALGIPTDPAAASNQLIQlldvhertGNWRRIGLIDCGEVWAIVN-AGVGVDAE 158
Cdd:TIGR00147  78 -IQLD----DIPALGILPLGTANDFARSLGIPEDLDKAAKLVIA--------GDARAIDMGQVNKQYCFINmAGGGFGTE 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063559289 159 VVAAVEE--KRRQGVKVTPLNYWRIA-----TPVSVRFsrrepnlilelpEREPIPGvHFAWVCNTNVWTYSSNRPMVtn 231
Cdd:TIGR00147 145 ITTETPEklKAALGSLSYILSGLMRMdtlqpFRCEIRG------------EGEHWQG-EAVVFLVGNGRQAGGGQKLA-- 209

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063559289 232 PGCSFETGL-GLFALTSMKLIPTIRLLrqLMAKRPKleakqLIRDDDVSYVRVTRMR--EPAAVQF--DGEYLG 300
Cdd:TIGR00147 210 PDASINDGLlDLRIFTNDNLLPALVLT--LMSDEGK-----HTDNPNIIYGKASRIDiqTPHKITFnlDGEPLG 276
 
Name Accession Description Interval E-value
LCB5 COG1597
Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, ...
 1-321 1.20e-57

Phosphatidylglycerol kinase, diacylglycerol kinase family [Lipid transport and metabolism, General function prediction only];


Pssm-ID: 441205 [Multi-domain]  Cd Length: 295  Bit Score: 187.75  E-value: 1.20e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063559289   1 MRAMLIVNPIATSITPA-ARELVAHALESR-VELTVEQTAYSGHAFELGKVAAADGYDLVVVHGGDGTVSAVVNGMLGRP 78
Cdd:COG1597     3 MRALLIVNPASGRGRAArLLERLVAALRAAgLEVEVLETESPGDATELAREAAAEGADLVVAAGGDGTVNEVANGLAGTG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063559289  79 dqaapdqlranvPAVGIIPGGSANVLARALGIPTDPAAASNQLIqlldvherTGNWRRIGLIDCGEVWAIVNAGVGVDAE 158
Cdd:COG1597    83 ------------PPLGILPLGTGNDFARALGIPLDPEAALEALL--------TGRTRRIDLGRVNGRYFLNVAGIGFDAE 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063559289 159 VVAAVEEKRRQgvKVTPLNYWRIAtpVSVRFSRREPNLILELPEREPIPGVHFAWVCNTNvwTYSSNrpMVTNPGCSFET 238
Cdd:COG1597   143 VVERANRALKR--RLGKLAYVLAA--LRALLRYRPFRLRIELDGEEIEGEALLVAVGNGP--YYGGG--LRLAPDASLDD 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063559289 239 G-LGLFALTSMKLIPTIRLLRQLMAKRpkleakqLIRDDDVSYVRVTRMR----EPAAVQFDGEYLGLRETMTFREVRDI 313
Cdd:COG1597   215 GlLDVVVVRPLSRLRLLRLLPRLLRGR-------HLRHPGVRYFRAREVEiesdRPLPVQLDGEPLGLATPLEFEVLPGA 287


                  ....*...
gi 1063559289 314 LPVVAPPS 321
Cdd:COG1597   288 LRVLVPAD 295
DAGK_cat pfam00781
Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts ...
 2-145 2.24e-31

Diacylglycerol kinase catalytic domain; Diacylglycerol (DAG) is a second messenger that acts as a protein kinase C activator. The catalytic domain is assumed from the finding of bacterial homologs. YegS is the Escherichia coli protein in this family whose crystal structure reveals an active site in the inter-domain cleft formed by four conserved sequence motifs, revealing a novel metal-binding site. The residues of this site are conserved across the family.


Pssm-ID: 425868 [Multi-domain]  Cd Length: 125  Bit Score: 114.22  E-value: 2.24e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063559289   2 RAMLIVNPiaTSITPAARELVAHA---LESR-VELTVEQTAYSGHAFELGKVAAADGYDLVVVHGGDGTVSAVVNGMLGR 77
Cdd:pfam00781   1 KLLVIVNP--KSGGGKGKKLLRKVrplLNKAgVEVELVLTEGPGDALELAREAAEDGYDRIVVAGGDGTVNEVLNGLAGL 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063559289  78 PDQaapdqlranvPAVGIIPGGSANVLARALGIPTDPAAASNQLIQlldvhertGNWRRiglIDCGEV 145
Cdd:pfam00781  79 ATR----------PPLGIIPLGTGNDFARALGIPGDPEEALEAILK--------GQTRP---VDVGKV 125
PRK00861 PRK00861
putative lipid kinase; Reviewed
 2-171 4.54e-20

putative lipid kinase; Reviewed


Pssm-ID: 234850 [Multi-domain]  Cd Length: 300  Bit Score: 88.53  E-value: 4.54e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063559289   2 RAMLIVNPIATSITPAAR-ELVAHALESRVELTVEQTAYSGHAFELGKVAAADGYDLVVVHGGDGTVSAVVNGMLGrpdq 80
Cdd:PRK00861    4 SACLIFNPVAGQGNPEVDlALIRAILEPEMDLDIYLTTPEIGADQLAQEAIERGAELIIASGGDGTLSAVAGALIG---- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063559289  81 aapdqlrANVPaVGIIPGGSANVLARALGIPTDPAAASNQLIQlldvhertGNWRRIGLIDCGEVWAIVNAGVGVDAEVV 160
Cdd:PRK00861   80 -------TDIP-LGIIPRGTANAFAAALGIPDTIEEACRTILQ--------GKTRRVDVAYCNGQPMILLAGIGFEAETV 143

                         170
                  ....*....|...
gi 1063559289 161 --AAVEEKRRQGV 171
Cdd:PRK00861  144 eeADREAKNRFGI 156
DAGKc smart00046
Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger ...
 5-127 1.29e-17

Diacylglycerol kinase catalytic domain (presumed); Diacylglycerol (DAG) is a second messenger that acts as a protein kinase C activator. DAG can be produced from the hydrolysis of phosphatidylinositol 4,5-bisphosphate (PIP2) by a phosphoinositide-specific phospholipase C and by the degradation of phosphatidylcholine (PC) by a phospholipase C or the concerted actions of phospholipase D and phosphatidate phosphohydrolase. This domain is presumed to be the catalytic domain. Bacterial homologues areknown.


Pssm-ID: 214487 [Multi-domain]  Cd Length: 124  Bit Score: 77.72  E-value: 1.29e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063559289    5 LIVNPIAT-----SITPAARELVAHALesrveltVEQTAYSGHAFELGKVAAADGYDLVVVHGGDGTVSAVVNGMLGRPD 79
Cdd:smart00046   2 VFVNPKSGggkgeKLLRKFRLLLNPRQ-------VFDLTKKGPAVALVIFRDVPDFNRVLVCGGDGTVGWVLNALDKREL 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1063559289   80 QAAPdqlranvPAVGIIPGGSANVLARALGIPTDPAAAsNQLIQLLDV 127
Cdd:smart00046  75 PLPE-------PPVAVLPLGTGNDLARSLGWGGGYDGE-KLLKTLRDA 114
PRK13055 PRK13055
putative lipid kinase; Reviewed
 1-122 1.23e-15

putative lipid kinase; Reviewed


Pssm-ID: 237282 [Multi-domain]  Cd Length: 334  Bit Score: 76.18  E-value: 1.23e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063559289   1 MRAMLIVNPiaTSITPAARELVAHALEsrvelTVEQTAYSGHAF----------ELGKVAAADGYDLVVVHGGDGTVSAV 70
Cdd:PRK13055    3 KRARLIYNP--TSGQEIMKKNVADILD-----ILEQAGYETSAFqttpepnsakNEAKRAAEAGFDLIIAAGGDGTINEV 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1063559289  71 VNGMlgrpdqaAPDQLRanvPAVGIIPGGSANVLARALGIPTDPAAASNQLI 122
Cdd:PRK13055   76 VNGI-------APLEKR---PKMAIIPAGTTNDYARALKIPRDNPVEAAKVI 117
PRK13337 PRK13337
putative lipid kinase; Reviewed
 2-113 1.28e-15

putative lipid kinase; Reviewed


Pssm-ID: 183982 [Multi-domain]  Cd Length: 304  Bit Score: 75.86  E-value: 1.28e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063559289   2 RAMLIVNPiaTSitpaARELVAHALeSRVELTVEQTAY---------SGHAFELGKVAAADGYDLVVVHGGDGTVSAVVN 72
Cdd:PRK13337    3 RARIIYNP--TS----GRELFKKNL-PDVLQKLEQAGYetsahattgPGDATLAAERAVERKFDLVIAAGGDGTLNEVVN 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1063559289  73 GMLGRPdqaapdqlraNVPAVGIIPGGSANVLARALGIPTD 113
Cdd:PRK13337   76 GIAEKE----------NRPKLGIIPVGTTNDFARALHVPRD 106
TIGR00147 TIGR00147
lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been ...
 2-300 2.97e-15

lipid kinase, YegS/Rv2252/BmrU family; The E. coli member of this family, YegS has been purified and shown to have phosphatidylglycerol kinase activity. The member from M. tuberculosis, Rv2252, has diacylglycerol kinase activity. BmrU from B. subtilis is in an operon with multidrug efflux transporter Bmr, but is uncharacterized. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 161732 [Multi-domain]  Cd Length: 293  Bit Score: 74.85  E-value: 2.97e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063559289   2 RAMLIVNPIA--TSITPAARELVAHALESRVELTVEQTAYSGHAFELGKVAAADGYDLVVVHGGDGTVSAVVNGMlgrpd 79
Cdd:TIGR00147   3 EAPAILNPTAgkSNDNKPLREVIMLLREEGMEIHVRVTWEKGDAARYVEEARKFGVDTVIAGGGDGTINEVVNAL----- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063559289  80 qAAPDqlraNVPAVGIIPGGSANVLARALGIPTDPAAASNQLIQlldvhertGNWRRIGLIDCGEVWAIVN-AGVGVDAE 158
Cdd:TIGR00147  78 -IQLD----DIPALGILPLGTANDFARSLGIPEDLDKAAKLVIA--------GDARAIDMGQVNKQYCFINmAGGGFGTE 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063559289 159 VVAAVEE--KRRQGVKVTPLNYWRIA-----TPVSVRFsrrepnlilelpEREPIPGvHFAWVCNTNVWTYSSNRPMVtn 231
Cdd:TIGR00147 145 ITTETPEklKAALGSLSYILSGLMRMdtlqpFRCEIRG------------EGEHWQG-EAVVFLVGNGRQAGGGQKLA-- 209

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063559289 232 PGCSFETGL-GLFALTSMKLIPTIRLLrqLMAKRPKleakqLIRDDDVSYVRVTRMR--EPAAVQF--DGEYLG 300
Cdd:TIGR00147 210 PDASINDGLlDLRIFTNDNLLPALVLT--LMSDEGK-----HTDNPNIIYGKASRIDiqTPHKITFnlDGEPLG 276
PRK13054 PRK13054
lipid kinase; Reviewed
 1-117 2.10e-14

lipid kinase; Reviewed


Pssm-ID: 237281 [Multi-domain]  Cd Length: 300  Bit Score: 72.21  E-value: 2.10e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063559289   1 MRAMLIVNPIATSiTPAARELVAHALESRVELTVEQTAYSGHAFELGKVAAADGYDLVVVHGGDGTVSAVVNGMLGRPDQ 80
Cdd:PRK13054    4 PKSLLILNGKSAG-NEELREAVGLLREEGHTLHVRVTWEKGDAARYVEEALALGVATVIAGGGDGTINEVATALAQLEGD 82

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1063559289  81 AapdqlranVPAVGIIPGGSANVLARALGIPTDPAAA 117
Cdd:PRK13054   83 A--------RPALGILPLGTANDFATAAGIPLEPDKA 111
PRK13057 PRK13057
lipid kinase;
4-171 2.16e-14

lipid kinase;


Pssm-ID: 183857 [Multi-domain]  Cd Length: 287  Bit Score: 72.26  E-value: 2.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063559289   4 MLIVNPIATSITPAARELVAHALESRVELTVEQTAYSGHAFELGKvAAADGYDLVVVHGGDGTVSAVVNGMLGRpdqaap 83
Cdd:PRK13057    1 LLLVNRHARSGRAALAAARAALEAAGLELVEPPAEDPDDLSEVIE-AYADGVDLVIVGGGDGTLNAAAPALVET------ 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063559289  84 dQLranvpAVGIIPGGSANVLARALGIPTDPAAASnQLIQlldvherTGNWRRiglIDCGEV--WAIVN-AGVGVDAEVV 160
Cdd:PRK13057   74 -GL-----PLGILPLGTANDLARTLGIPLDLEAAA-RVIA-------TGQVRR---IDLGWVngHYFFNvASLGLSAELA 136

                         170
                  ....*....|...
gi 1063559289 161 AAV--EEKRRQGV 171
Cdd:PRK13057  137 RRLtkELKRRWGT 149
PRK12361 PRK12361
hypothetical protein; Provisional
 2-171 1.34e-12

hypothetical protein; Provisional


Pssm-ID: 183473 [Multi-domain]  Cd Length: 547  Bit Score: 68.11  E-value: 1.34e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063559289   2 RAMLIVNPIA-TSITPAARELVAHALESRVELTVEQTAYSGHAFELGKVAAADGYDLVVVHGGDGTVSAVVNGMLGRPDQ 80
Cdd:PRK12361  244 RAWLIANPVSgGGKWQEYGEQIQRELKAYFDLTVKLTTPEISAEALAKQARKAGADIVIACGGDGTVTEVASELVNTDIT 323

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063559289  81 aapdqlranvpaVGIIPGGSANVLARAL-GIPTDPAAASNQLIQLLDvhertGNWRRIGLIDCGEVWAIVNAGVGVDAEV 159
Cdd:PRK12361  324 ------------LGIIPLGTANALSHALfGLGSKLIPVEQACDNIIQ-----GHTQRIDTARCNDRLMLLLVGIGFEQKM 386

                         170
                  ....*....|....
gi 1063559289 160 V--AAVEEKRRQGV 171
Cdd:PRK12361  387 IesADRERKNALGQ 400
PRK13059 PRK13059
putative lipid kinase; Reviewed
 53-123 5.39e-10

putative lipid kinase; Reviewed


Pssm-ID: 183858  Cd Length: 295  Bit Score: 59.28  E-value: 5.39e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063559289  53 DGYDLVVVHGGDGTVSAVVNGMLgrpdqaapdQLRANVPaVGIIPGGSANVLARALGIPTDPAAASNQLIQ 123
Cdd:PRK13059   55 ESYKYILIAGGDGTVDNVVNAMK---------KLNIDLP-IGILPVGTANDFAKFLGMPTDIGEACEQILK 115
PRK11914 PRK11914
diacylglycerol kinase; Reviewed
 2-159 1.13e-09

diacylglycerol kinase; Reviewed


Pssm-ID: 237021 [Multi-domain]  Cd Length: 306  Bit Score: 58.64  E-value: 1.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063559289   2 RAMLIVNPIAT--SITPAARELVAHALESRVELTVEQTAYSGHAFELGKVAAADGYDLVVVHGGDGTVSAVVNGMLGrpd 79
Cdd:PRK11914   10 KVTVLTNPLSGhgAAPHAAERAIARLHHRGVDVVEIVGTDAHDARHLVAAALAKGTDALVVVGGDGVISNALQVLAG--- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063559289  80 qaapdqlrANVPaVGIIPGGSANVLARALGIPT-DPAAASNQLIqllDVHERTGNWRRIGLIDCGEVWAIVNAGVGVDAE 158
Cdd:PRK11914   87 --------TDIP-LGIIPAGTGNDHAREFGIPTgDPEAAADVIV---DGWTETVDLGRIQDDDGIVKWFGTVAATGFDSL 154


                  .
gi 1063559289 159 V 159
Cdd:PRK11914  155 V 155
PLN02958 PLN02958
diacylglycerol kinase/D-erythro-sphingosine kinase
 2-131 2.31e-09

diacylglycerol kinase/D-erythro-sphingosine kinase


Pssm-ID: 215517 [Multi-domain]  Cd Length: 481  Bit Score: 58.33  E-value: 2.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063559289   2 RAMLIVNPIA--TSITPAARELVAHALE-SRVELTVEQTAYSGHAFELGKVAAADGYDLVVVHGGDGTVSAVVNGMLGRP 78
Cdd:PLN02958  113 RLLVFVNPFGgkKSASKIFFDVVKPLLEdADIQLTIQETKYQLHAKEVVRTMDLSKYDGIVCVSGDGILVEVVNGLLERE 192

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1063559289  79 DQAAPDQLranvpAVGIIPGGSANVLARALGIPT-DPAAASNQLIQLLDVHERT 131
Cdd:PLN02958  193 DWKTAIKL-----PIGMVPAGTGNGMAKSLLDSVgEPCSATNAVLAIIRGHKCS 241
NadK COG0061
NAD kinase [Coenzyme transport and metabolism];
1-95 1.65e-03

NAD kinase [Coenzyme transport and metabolism];


Pssm-ID: 439831 [Multi-domain]  Cd Length: 279  Bit Score: 39.35  E-value: 1.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063559289   1 MRAMLIV-NPIATSITPAARELVAHALESRVELTVEQ-TAYSGHAFElgkvAAADGYDLVVVHGGDGTvsavvngMLgrp 78
Cdd:COG0061     1 MKRIAIVaKPGKPEALEAAEELAELLEERGIEVVLDEdTAVPGVPLE----ELGEEADLVIVLGGDGT-------LL--- 66

                          90
                  ....*....|....*..
gi 1063559289  79 dQAAPDQLRANVPAVGI 95
Cdd:COG0061    67 -RAARLLAPLGIPILGI 82
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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